ID   DPOL_HHV8P              Reviewed;        1012 AA.
AC   Q2HRD0;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   23-FEB-2022, entry version 84.
DE   RecName: Full=DNA polymerase catalytic subunit;
DE            EC=2.7.7.7;
DE            EC=3.1.26.4;
GN   Name=ORF9;
OS   Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's
OS   sarcoma-associated herpesvirus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Rhadinovirus.
OX   NCBI_TaxID=868565;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10400794; DOI=10.1128/jvi.73.8.6953-6963.1999;
RA   Glenn M., Rainbow L., Aurade F., Davison A., Schulz T.F.;
RT   "Identification of a spliced gene from Kaposi's sarcoma-associated
RT   herpesvirus encoding a protein with similarities to latent membrane
RT   proteins 1 and 2A of Epstein-Barr virus.";
RL   J. Virol. 73:6953-6963(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16760382; DOI=10.1099/vir.0.81919-0;
RA   Rezaee S.A.R., Cunningham C., Davison A.J., Blackbourn D.J.;
RT   "Kaposi's sarcoma-associated herpesvirus immune modulation: an overview.";
RL   J. Gen. Virol. 87:1781-1804(2006).
CC   -!- FUNCTION: Replicates viral genomic DNA. The replication complex is
CC       composed of six viral proteins: the DNA polymerase, processivity
CC       factor, primase, primase-associated factor, helicase, and ssDNA-binding
CC       protein. Additionally, the polymerase contains an intrinsic
CC       ribonuclease H (RNase H) activity that specifically degrades RNA/DNA
CC       heteroduplexes or duplex DNA substrates in the 5' to 3' direction.
CC       Therefore, it can catalyze the excision of the RNA primers that
CC       initiate the synthesis of Okazaki fragments at a replication fork
CC       during viral DNA replication (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC         diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC         Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC         ChEBI:CHEBI:173112; EC=2.7.7.7;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC   -!- SUBUNIT: Forms a complex with the ssDNA-binding protein, the DNA
CC       polymerase processivity factor, and the alkaline exonuclease. Interacts
CC       with the putative helicase-primase complex subunit; this interaction
CC       may coordinate leading and lagging strand DNA synthesis at the
CC       replication fork (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000305}. Note=The protein is
CC       present at discrete sites in nuclei, called replication compartments
CC       where viral DNA replication occurs. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B family. {ECO:0000305}.
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DR   EMBL; AF148805; ABD28853.1; -; Genomic_DNA.
DR   RefSeq; YP_001129355.1; NC_009333.1.
DR   SMR; Q2HRD0; -.
DR   PRIDE; Q2HRD0; -.
DR   DNASU; 4961513; -.
DR   GeneID; 4961513; -.
DR   KEGG; vg:4961513; -.
DR   Proteomes; UP000000942; Genome.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-EC.
DR   GO; GO:0039686; P:bidirectional double-stranded viral DNA replication; IDA:UniProtKB.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.132.60; -; 1.
DR   Gene3D; 3.30.420.10; -; 1.
DR   Gene3D; 3.90.1600.10; -; 1.
DR   InterPro; IPR006172; DNA-dir_DNA_pol_B.
DR   InterPro; IPR017964; DNA-dir_DNA_pol_B_CS.
DR   InterPro; IPR006133; DNA-dir_DNA_pol_B_exonuc.
DR   InterPro; IPR006134; DNA-dir_DNA_pol_B_multi_dom.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR042087; DNA_pol_B_thumb.
DR   InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   Pfam; PF00136; DNA_pol_B; 1.
DR   Pfam; PF03104; DNA_pol_B_exo1; 1.
DR   PRINTS; PR00106; DNAPOLB.
DR   SMART; SM00486; POLBc; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE   3: Inferred from homology;
KW   DNA replication; DNA-binding; DNA-directed DNA polymerase; Endonuclease;
KW   Host nucleus; Hydrolase; Multifunctional enzyme; Nuclease;
KW   Nucleotidyltransferase; Reference proteome; Transferase;
KW   Viral DNA replication.
FT   CHAIN           1..1012
FT                   /note="DNA polymerase catalytic subunit"
FT                   /id="PRO_0000423802"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1012 AA;  113326 MW;  85630925BD54CC9C CRC64;
     MDFFNPFIDP TRGGPRNTVR QPTPSQSPTV PSETRVCRLI PACFQTPGRP GVVAVDTTFP
     PTYFQGPKRG EVFAGETGSI WKTRRGQARN APMSHLIFHV YDIVETTYTA DRCEDVPFSF
     QTDIIPSGTV LKLLGRTLDG ASVCVNVFRQ RCYFYTLAPQ GVNLTHVLQQ ALQAGFGRAS
     CGFSTEPVRK KILRAYDTQQ YAVQKITLSS SPMMRTLSDR LTTCGCEVFE SNVDAIRRFV
     LDHGFSTFGW YECSNPAPRT QARDSWTELE FDCSWEDLKF IPERTEWPPY TILSFDIECM
     GEKGFPNATQ DEDMIIQISC VLHTVGNDKP YTRMLLGLGT CDPLPGVEVF EFPSEYDMLA
     AFLSMLRDYN VEFITGYNIA NFDLPYIIAR ATQVYDFKLQ DFTKIKTGSV FEVHQPRGGS
     DGGNFMRSQS KVKISGIVPI DMYQVCREKL SLSDYKLDTV AKQCLGRQKD DISYKDIPPL
     FKSGPDGRAK VGNYCVIDSV LVMDLLLRFQ THVEISEIAK LAKIPTRRVL TDGQQIRVFS
     CLLEAAATEG YILPVPKGDA VSGYQGATVI SPSPGFYDDP VLVVDFASLY PSIIQAHNLC
     YSTLIPGDSL HLHPHLSPDD YETFVLSGGP VHFVKKHKRE SLLAKLLTVW LAKRKEIRKT
     LASCTDPALK TILDKQQLAI KVTCNAVYGF TGVASGILPC LNIAETVTLQ GRKMLERSQA
     FVEAISPERL AGLLRRPVDV SPDARFKVIY GDTDSLFICC MGFNMDSVSD FAEELASITT
     NTLFRSPIKL EAEKIFKCLL LLTKKRYVGV LSDDKVLMKG VDLIRKTACR FVQEKSSQVL
     DLILREPSVK AAAKLISGQA TDWVYREGLP EGFVKIIQVL NASHRELCER SVPVDKLTFT
     TELSRPLADY KTQNLPHLTV YQKLQARQEE LPQIHDRIPY VFVDAPGSLR SELAEHPEYV
     KQHGLRVAVD LYFDKLVHAV ANIIQCLFQN NTSATVAILY NFLDIPVTFP TP